Related ArticlesExploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):773-80
Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B
Putidaredoxin is a di-iron protein whose paramagnetic region is not well characterized by 1H detected NMR. We have studied the structure of this region in greater detail by directly observed 15N NMR of oxidized and reduced putidaredoxin preparations in which the six cysteine residues are selectively labeled with 15N. A new method for preparation of a stable form of reduced putidaredoxin has been developed for use in NMR. The 15N NMR spectra of the oxidized and reduced forms are characteristically different, and we have measured and compared 15N chemical shifts, spin-lattice relaxation times (T1), and chemical shift/temperature dependences for both forms. Evidence for localized valencies of the iron atoms in the reduced form is presented. From the 15N T1 values of the oxidized form, reduced distances of the cysteine backbone 15N nuclei from the center of the Fe2S2 cluster have been calculated. These distances are consistent with those calculated from X-ray crystal structure data for five ferredoxins, and confirm the structural similarity of the Fe2S2 clusters in putidaredoxin and in these ferredoxins in the oxidized state.
[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
Related Articles Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
J Mol Biol. 2004 Nov 19;344(2):567-83
Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA
IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...
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[NMR paper] Identification of slow motions in the reduced recombinant high-potential iron sulfur
Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
Related Articles Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
J Biomol NMR. 1998 Aug;12(2):307-18
Authors: Banci L, Felli IC, Koulougliotis D
Rotating-frame 15N relaxation rate (R1 rho) NMR experiments have been...
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[NMR paper] 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhod
1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans.
Eur J Biochem. 1996 Mar 1;236(2):405-11
Authors: Ciurli S, Cremonini MA, Kofod P, Luchinat C
Oxidized and reduced forms of high-potential iron-sulfur protein (HiPIP) from the...
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[NMR paper] Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron p
Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Related Articles Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Biochemistry. 1995 Dec 5;34(48):15646-53
Authors: Lanzilotta WN, Holz RC, Seefeldt LC
This work presents the complete assignment of the isotropically shifted 1H NMR resonances of Azotobacter vinelandii...
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[NMR paper] Three-dimensional solution structure of the oxidized high potential iron-sulfur prote
Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species.
Related Articles Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species.
Biochemistry. 1995 Aug 8;34(31):9851-8
Authors: Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P
The NMR solution structure of...
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[NMR paper] 1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus t
1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure.
Related Articles 1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure.
Biochemistry. 1995 Jan 17;34(2):600-10
Authors: Gorst CM, Yeh YH, Teng Q, Calzolai L, Zhou ZH, Adams MW, La Mar GN
One- and two-dimensional 1H NMR...
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[NMR paper] The three-dimensional solution structure of the reduced high-potential iron-sulfur pr
The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
Related Articles The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
Biochemistry. 1995 Jan 10;34(1):206-19
Authors: Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P
The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature has been extended up to 85% of the total protein protons. Ninety...
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[NMR paper] 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from
1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.
Eur J Biochem. 1993 Feb 15;212(1):69-78
Authors: Bertini I, Capozzi F, Luchinat C, Piccioli M
1H one-dimensional and two-dimensional NMR spectra have been...